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Small-Angle X-ray Scattering Study of Changes in the Quaternary Structure of Nucleotide-Regulated Pyrophosphatase from Desulfitobacterium hafniense upon Ligand Binding in Solutionстатья Исследовательская статья
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 25 ноября 2020 г.
- Авторы: Dadinova L.A., Anashkin V.A., Shtykova E.V.
- Журнал: Crystallography Reports
- Том: 65
- Номер: 5
- Год издания: 2020
- Издательство: Maik Nauka/Interperiodica Publishing
- Местоположение издательства: Russian Federation
- Первая страница: 749
- Последняя страница: 754
- DOI: 10.1134/S1063774520050053
- Аннотация: The regulation of nucleotide-regulated inorganic pyrophosphatases at a molecular level has been extensively studied in order to establish the mechanism of signal transduction between the active and regulatory sites of these enzymes. However, this issue cannot be ultimately addressed because of the lack of reliable structural data on the full-length protein and its interactions with ligands. The low-resolution structure of nucleotide-regulated pyrophosphatase from Desulfitobacterium hafniense was determined for the first time by small-angle X-ray scattering. The structural changes in the full-length enzyme upon binding of adenosine monophosphate and diadenosine tetraphosphate were revealed. In dilute solutions the protein was found to exist as a stable homotetramer, the structure of which depends on the nature of the bound ligand. The structural data are important for an understanding of the molecular basis for regulation of this family of enzymes.
- Добавил в систему: Анашкин Виктор Андреевич